CJC-1295 No DAC: Research Overview of GHRH Analogue

CJC-1295 No DAC (Drug Affinity Complex) is a modified 29-amino-acid growth hormone-releasing hormone (GHRH) analog used in laboratory research. It differs from clinical formulations by lacking the albumin-binding “DAC” moiety, making it short-acting. In preclinical settings, CJC-1295 No DAC binds the GHRH receptor to drive pulsatile GH release, aiding studies of GH/IGF-1 signaling and endocrine pathways【26†L130-L139】【33†L175-L183】. All applications of CJC-1295 No DAC must be strictly research-use only.

Fast Answer

Structural Features and Analog Comparisons

CJC-1295 No DAC is often called modified GRF 1-29, indicating four amino-acid substitutions relative to native GHRH (GHRH(1-29)) that enhance stability【48†L166-L174】【11†L197-L200】. Notably, position 2 is substituted with D-Ala, which resists DPP-IV cleavage and increases half-life【11†L197-L200】. Other substitutions further protect against metabolic degradation. Unlike CJC-1295 with DAC, this peptide has no albumin-binding extension, so its in vivo half-life is on the order of tens of minutes (versus days for the DAC version)【26†L130-L139】【11†L197-L200】.

The table above compares key GHRH analogs. CJC-1295 No DAC’s modifications (second row) make it more stable than unmodified GHRH, yet it remains far more transient than the albumin-conjugated CJC-1295 (third row). This pulsatile profile may be preferred in studies of physiological GH signaling.

Mechanism of GHRH Analog Action

CJC-1295 No DAC functions by activating the GHRH receptor (GHRHR) on pituitary somatotroph cells. Binding triggers a G_s-protein cascade: adenylyl cyclase converts ATP to cAMP, which then activates protein kinase A (PKA). PKA phosphorylation leads to vesicular release of stored growth hormone (GH)【26†L130-L139】. The secreted GH enters circulation and acts on peripheral tissues (notably the liver) to induce insulin-like growth factor 1 (IGF-1) synthesis. In research models, this is typically measured as a surge in GH, often followed by a smaller rise in IGF-1【26†L130-L139】. The following diagram outlines this signaling pathway:

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Pharmacokinetics and Stability

Native GHRH (1-29) has an extremely short half-life (minutes) due to rapid enzymatic degradation by peptidases such as DPP-IV【11†L197-L200】. The D-Ala² substitution in CJC-1295 No DAC is known to hinder DPP-IV cleavage, lengthening the peptide’s half-life approximately to ~30 minutes【11†L197-L200】. Additional substitutions at positions 8, 15, and 27 further improve stability against other proteases. However, without the albumin binder (DAC), the peptide is still cleared relatively quickly. In contrast, adding an albumin-binding group (as in CJC-1295 with DAC) dramatically extends circulation time to several days【26†L130-L139】. Researchers should note these kinetic differences when designing experiments: CJC-1295 No DAC leads to short GH pulses, whereas DAC-conjugated versions provide more sustained GH elevation.

Because CJC-1295 No DAC is not metabolized over long periods, its stimulation of GH release typically results in a transient GH peak. In small clinical studies of long-acting GHRH analogs, a single dose raised GH levels 2–10-fold for ~6 days and IGF-1 1.5–3-fold for ~9–11 days【26†L130-L139】. The No DAC variant would be expected to produce a far shorter effect, resembling a normal hypothalamic GH pulse. All such outcomes in literature are framed as observations in research subjects, not as therapeutic results.

Research Applications and Analytical Considerations

Researchers use CJC-1295 No DAC primarily as a tool to probe GH/IGF-1 endocrine pathways in vitro and in vivo. Typical studies include pituitary cell assays, tissue explants, and animal models where GH secretion dynamics are of interest. Its short action can be useful for studying GH pulsatility or as a control ligand in receptor assays. Because this compound is strictly for research, experimental design often involves multiple lab-scale doses or continuous infusion protocols to mimic physiological patterns, and always within controlled preclinical contexts.

Analytical Testing and Quality Control: Laboratories verify peptide identity and purity using standard analytical techniques. Reverse-phase HPLC is commonly used to assess purity, and mass spectrometry (LC-MS/MS) confirms molecular weight and sequence. For example, forensic analyses of GHRH analogs (including CJC-1295 variants) have used spiked reference standards and sensitive LC-MS/MS methods to detect analogs and metabolites at ng/mL levels【32†L57-L66】. In a research lab, establishing a Certificate of Analysis (COA) is essential: it should include HPLC purity data, MS identity, and chromatographic/mass spectra. Validated reference peptides or internal standards ensure each batch meets expected specifications. Researchers should always review batch-specific documentation (COA) to confirm purity (typically ≥95%) and identity before use.

Example Laboratory Workflow:

“`mermaid flowchart TD X[Request RUO peptide (e.g., CJC-1295 No DAC)] –> Y[Receive COA and peptide vial] Y –> Z[Verify identity (LC-MS) and purity (HPLC)] Z –> W{Meets quality standards?} W — Yes –> R[Use peptide for GH release studies] W — No –> S[Contact supplier / discard batch] “`

This workflow highlights the typical steps from obtaining to confirming a research peptide before use in experiments.

Evidence Overview

Published data specific to CJC-1295 No DAC are limited, but related literature provides context. Early analog studies showed that serum-stabilized GHRH peptides can significantly boost GH output. For example, an albumin-conjugated tetrasubstituted GHRH analog (CJC-1295) in rats produced a ~3-fold greater GH area-under-curve than native GHRH【33†L175-L183】. In humans, long-acting CJC-1295 formulations led to multi-day GH and IGF-1 elevations【26†L130-L139】. By analogy, CJC-1295 No DAC is expected to elicit a short-term GH pulse without prolonged IGF-1 effect. No reliable clinical outcomes or dosing studies exist for the No DAC variant, underscoring that its role is purely experimental. All available findings come from controlled research assays or small animal models, with careful attention to context and limitations.

FAQs

What is CJC-1295 No DAC?

CJC-1295 No DAC is a 29-residue synthetic peptide analog of human growth hormone-releasing hormone (GHRH) engineered for research use. It includes multiple amino-acid substitutions to extend stability compared to native GHRH【11†L197-L200】. The “No DAC” designation means it lacks the albumin-binding domain used in some formulations. Researchers use it to study GHRH receptor signaling and GH release in preclinical models.

How does CJC-1295 No DAC work in research?

In laboratory studies, CJC-1295 No DAC binds to the GHRH receptor on pituitary cells, triggering the usual GHRH signaling cascade. This leads to transient growth hormone (GH) release into the blood, similar to a natural GH pulse【26†L130-L139】. The short half-life of the peptide means GH levels rise briefly. Researchers measure this response (and subsequent IGF-1 changes) as an indicator of GHRH pathway activity.

Why is it called “No DAC”?

The term “DAC” stands for Drug Affinity Complex, a chemical group that can be added to peptides to extend their half-life by binding serum albumin. CJC-1295 No DAC simply lacks this albumin-binding group. It retains other stabilizing modifications (D-Ala², etc.) but is not attached to a carrier. As a result, it has a much shorter in vivo half-life (minutes) compared to CJC-1295 with DAC (days)【26†L130-L139】【11†L197-L200】.

How is CJC-1295 No DAC analyzed in the lab?

Researchers verify CJC-1295 No DAC identity and purity using chromatographic and spectrometric methods. A typical approach is to run the peptide on reverse-phase HPLC (often with UV detection) to check purity. Mass spectrometry (LC-MS/MS) is then used to confirm the correct molecular weight/sequence. These methods are standard for quality control: for instance, forensic labs have developed LC-MS assays to detect GHRH analogs at ng/mL levels【32†L57-L66】. The results form part of the peptide’s certificate of analysis.

What does research say about CJC-1295 No DAC effects?

Specific studies on CJC-1295 No DAC itself are scarce. However, related GHRH analogs demonstrate the expected biology: modified GHRH peptides increase GH release more than native GHRH in test systems【33†L175-L183】. In small trials of the DAC version, single doses raised GH 2–10× and IGF-1 1.5–3× in humans【26†L130-L139】. By extension, CJC-1295 No DAC is presumed to cause a brief GH surge; any use is limited to cell/tissue or animal models. All available data are preclinical or from controlled experiments, and outcomes should be interpreted with caution.

Next Steps

Before selecting any RUO peptide, review batch-specific documentation such as certificates of analysis and purity data. For CJC-1295 No DAC and other research peptides, Pure Lab Peptides provides clear labeling and available test data to support scientific use. Researchers should prioritize transparent product information and quality control when choosing peptides for their studies.

References

1. Teichman SL, Neale A, Lawrence B, Gagnon C, Castaigne JP, Frohman LA. “Prolonged stimulation of growth hormone (GH) and insulin-like growth factor I secretion by CJC-1295, a long-acting analog of GH-releasing hormone, in healthy adults.” J Clin Endocrinol Metab. 2006;91(3):799–805. doi.org/10.1210/jc.2005-1536
2. Memdouh S, Gavrilović I, Ng K, Cowan D, Abbate V. “Advances in the detection of growth hormone releasing hormone synthetic analogs.” Drug Test Anal. 2021;13(11-12):1871–1887. doi.org/10.1002/dta.3183
3. Jetté L, Léger R, Thibaudeau K, et al. “Human growth hormone-releasing factor (hGRF)1–29-albumin bioconjugates activate the GRF receptor on the anterior pituitary in rats: identification of CJC-1295 as a long-lasting GRF analog.” Endocrinology. 2005;146(7):3052–3058. doi.org/10.1210/en.2004-1286
4. Soule S, King JA, Millar RP. “Incorporation of D-Ala² in growth hormone-releasing hormone-(1-29)-NH₂ increases the half-life and decreases metabolic clearance in normal men.” J Clin Endocrinol Metab. 1994;79(4):1208–1211. doi.org/10.1210/jcem.79.4.7962295